Thermo Fisher Scientific ADAM23 Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500-1:1,000

-

Product Specifications

Species Reactivity

Human, Mouse

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

Synthesized peptide derived from human ADAM23. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:ADAM23,uniProtId:O75077-1,ncbiNodeId:9606,antigenRange:765-792,antigenLength:832,antigenImageFileName:PA5-68083_ADAM23_O75077-1_Rabbit.svg,antigenImageFileNamePDP:PA5-68083_ADAM23_O75077-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

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Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

affinity chromatography

Storage buffer

PBS, pH 7.3, with 30% glycerol

Contains

0.01% sodium azide

Storage conditions

-20°C

Shipping conditions

Wet ice

RRID

AB_2691642

Product Specific Information

Predicted to react with Mouse samples.

Target Information

ADAMs (a disintegrin and metalloproteinase domain), also known as MDCs (metalloproteinase, disintegrin, and cysteine-rich domain) or cellular disintegrins, are a family of proteins that are expressed in numerous different tissues. They catalyze proteolysis, adhesion, fusion and intracellular signaling. ADAMs are membrane-anchored proteins, and there are over 30 different members in the family with many diverse functions. ADAM 23 is exclusively expressed in fetal and adult brain and may function as an integrin ligand in cells of neural origin. Adhesion of neuroblastoma and astrocytoma cells is promoted by the disentegrin-like domain of ADAM23 and is mediated by an interaction of this protein with αvβ3. A short amino acid sequence in the disintegrin loop of ADAM23 interacts with αvβ3 to mediate cell interactions that take place during both normal and pathological processes. The three characteristic histidine residues and the glutamic acid residue typical of metalloproteinases are lacking in the metalloproteinase-like domain of ADAM23. This suggests that ADAM23 may not be involved in protease-mediated events, but could exclusively serve in cell adhesion processes. In addition, evidence suggests that ADAM23 may be a tumor suppressor gene.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.